1.7.3.3: factor-independent urate hydroxylase
This is an abbreviated version!
For detailed information about factor-independent urate hydroxylase, go to the full flat file.

Word Map on EC 1.7.3.3
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1.7.3.3
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hyperuricemia
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renal
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peroxisomal
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allopurinol
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xanthine
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purine
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allantoin
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gout
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catalase
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electrode
-
oxonic
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biosensors
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hematologic
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prophylaxis
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hypoxanthine
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febuxostat
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allantoinase
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hyperkalemia
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flavus
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uricosuric
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ureide
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amperometric
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hypocalcemia
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pegylated
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hyperphosphatemia
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urate-lowering
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methemoglobinemia
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microbodies
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probenecid
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tophi
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hominoid
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hypouricemic
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benzbromarone
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phosphotungstate
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utilis
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pimecrolimus
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pharmacology
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darbepoetin
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drug development
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nodule-specific
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medicine
-
analysis
-
synthesis
- 1.7.3.3
- hyperuricemia
- renal
- peroxisomal
- allopurinol
- xanthine
- purine
- allantoin
- gout
- catalase
-
electrode
-
oxonic
-
biosensors
-
hematologic
-
prophylaxis
- hypoxanthine
- febuxostat
- allantoinase
- hyperkalemia
- flavus
-
uricosuric
-
ureide
-
amperometric
-
hypocalcemia
-
pegylated
- hyperphosphatemia
-
urate-lowering
- methemoglobinemia
- microbodies
- probenecid
-
tophi
-
hominoid
-
hypouricemic
- benzbromarone
-
phosphotungstate
- utilis
- pimecrolimus
- pharmacology
-
darbepoetin
- drug development
-
nodule-specific
- medicine
- analysis
- synthesis
Reaction
Synonyms
AaUO, AgUOX, ELITEK, Fasturtec, N-35, Nodule specific uricase, Nodulin 35, Nodulin 35 homolog, Non-symbiotic uricase, oxidase, urate, Rasburicase, Uaz, Uox, Urate oxidase, urate oxidoreductase, UriA, uric acid oxidase, uricase, uricase II, Uricoenzyme, Uricozyme
ECTree
Advanced search results
Results
in table
3
4412
187
91
196
16
161
45
64
Engineering
Engineering on EC 1.7.3.3 - factor-independent urate hydroxylase
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L171I/Y182F/Y187F/A193S
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mutant displays higher activity and lower thermostability
L322R
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mutant shows reduced activity and thermal stability at pH 7.4, enhanced stability at pH 9.2
R310E
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displays the lowest stability at pH 7.4 or 9.2 among tested mutants and the strongest effects of pH values on thermal stability
S314Stop
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mutant is a homotetramer of about 25% activity, 5 % half-life at pH 7.4 but 100 % half-life at pH 9.2
Y249F
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thermal stability is reduced by 50fold at pH 7.4, by about 7fold at pH 9.2
Y319F
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thermal stability is reduced by one magnitude at pH 7.4, but by 2fold at pH 9.2
R310E
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displays the lowest stability at pH 7.4 or 9.2 among tested mutants and the strongest effects of pH values on thermal stability
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Y249F
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thermal stability is reduced by 50fold at pH 7.4, by about 7fold at pH 9.2
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Y319F
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thermal stability is reduced by one magnitude at pH 7.4, but by 2fold at pH 9.2
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K9M
T69A
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mutant enzyme has a maximal velocity of 3% of the wild-type value. Ionization at pH 6.4 that is observed with the wild-type enzyme is absent in the mutant. The KM-value for urate is 5fold higher than that of the wild-type enzyme
T69A/K9M
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the KM-value for urate is 16.1fold higher than that of the wild-type enzyme
T69V
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the KM-value for urate is 30.9fold higher than that of the wild-type enzyme
A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. About 30% of wild-type catalytic efficiency
H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. Catalytic efficiency is higher than in wild-type, but below the efficiency of mutant R291K/A296V/A301S/K303R
I115V/H119R/L120F/H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme, complete loss of activity
R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. About 50% increase in catalytic efficiency
synthesis
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expression of baboon uricase gene attached with Trx and hexahistidine tags in Escherichia coli Rosetta (DE3). The final yield of mature baboon uricase is 136.0 mg/l with enzyme activity of 17.93 U/mg
additional information
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mutant enzyme has a maximal velocity of 0.4% of the wild-type value. Ionization at pH 6.4 that is observed with the wild-type enzyme is absent in the mutant. The KM-value for urate is 1.5fold higher than that of the wild-type enzyme
K9M
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mutant is not able to generate the dianion of urate and is decreased in activity by over 200-fold
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uricase covalently linked to monomethoxypoly(ethylene glycol) N-leucine-OSu, branched monomethoxypoly(ethylene glycol) N-leucine-OSu or poly(N-acryloylmorpholine)-OSu last longer in blood
additional information
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the folding of the C-terminal residues is crucial for thermal stability. When positive charge on residue R3 is eliminated, the mutants become inactive dimers
additional information
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the folding of the C-terminal residues is crucial for thermal stability. When positive charge on residue R3 is eliminated, the mutants become inactive dimers
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additional information
the recombinantly expressed porcine enzyme, with a C-terminal sequence from baboon uricase, is applicated to patients with refractory gout, due to a mutation in the uricase gene, by intravenous injection in a PEG-bound form, pharmacokinetics and pharmacodynamics, safety, and efficacy of the treatment in a clinical trial, overview